Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2008-5-16
pubmed:abstractText
ATP is an extracellular signaling molecule that activates specific G protein-coupled P2Y receptors in most cell types to mediate diverse biological effects. ATP has been shown to activate the phospholipase C (PLC)/diacylglycerol/protein kinase C (PKC) pathway in various systems. However, little is known about the signaling events in human endometrial stromal cells (hESCs). The objective of this study was to examine the presence of the P2Y2 receptor and the effects of exogenous ATP on the intracellular mitogen-activated protein kinases (MAPKs) signaling pathway, immediate early genes expression, and cell viability in hESCs. Western blot analysis, gene array analysis, and MTT assay for cell viability were performed. The current study demonstrated the existence of the P2Y2 purinergic receptor in hESCs. UTP and ATP activated MAPK in a dose- and time-dependent manner. Suramin (a P2-purinoceptor antagonist), neomycin (a PLC inhibitor), staurosporin (a PKC inhibitor), and PD98059 (a MEK inhibitor) significantly attenuated the ATP-induced activation of MAPK. ATP activated ERK1/2 and induced translocation of activated ERK1/2 to the nucleus. The gene array for 23 genes associated with members of the mitogenic pathway cascade and immediate early genes revealed that the expression of early growth response 1 was increased. In addition, MTT assay revealed an inhibition effect of ATP on cell viability. ATP activated MAPKs through the P2Y2 purinoceptor/PLC/PKC/ERK signaling pathway and induced translocation of ERK1/2 into the nucleus. Further, ATP induced the expression of early growth response 1 and inhibited cell viability in hESCs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0898-6568
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1248-55
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:18434089-Adenosine Triphosphate, pubmed-meshheading:18434089-Adult, pubmed-meshheading:18434089-Cell Nucleus, pubmed-meshheading:18434089-Cell Proliferation, pubmed-meshheading:18434089-Cell Survival, pubmed-meshheading:18434089-Early Growth Response Protein 1, pubmed-meshheading:18434089-Endometrium, pubmed-meshheading:18434089-Enzyme Activation, pubmed-meshheading:18434089-Extracellular Signal-Regulated MAP Kinases, pubmed-meshheading:18434089-Extracellular Space, pubmed-meshheading:18434089-Female, pubmed-meshheading:18434089-Humans, pubmed-meshheading:18434089-MAP Kinase Signaling System, pubmed-meshheading:18434089-Mitogen-Activated Protein Kinase Kinases, pubmed-meshheading:18434089-Oligonucleotide Array Sequence Analysis, pubmed-meshheading:18434089-Protein Kinase C, pubmed-meshheading:18434089-Protein Transport, pubmed-meshheading:18434089-Receptors, Purinergic P2, pubmed-meshheading:18434089-Receptors, Purinergic P2Y2, pubmed-meshheading:18434089-Stromal Cells, pubmed-meshheading:18434089-Type C Phospholipases, pubmed-meshheading:18434089-Uridine Triphosphate
pubmed:year
2008
pubmed:articleTitle
Extracellular ATP activates the PLC/PKC/ERK signaling pathway through the P2Y2 purinergic receptor leading to the induction of early growth response 1 expression and the inhibition of viability in human endometrial stromal cells.
pubmed:affiliation
Graduate Institute of Medical Sciences, College of Medicine, Taipei Medical University, Taiwan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't